MOT1_HUMAN - dbPTM
MOT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MOT1_HUMAN
UniProt AC P53985
Protein Name Monocarboxylate transporter 1
Gene Name SLC16A1
Organism Homo sapiens (Human).
Sequence Length 500
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Proton-coupled monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate. Depending on the tissue and on cicumstances, mediates the import or export of lactic acid and ketone bodies. Required for normal nutrient assimilation, increase of white adipose tissue and body weight gain when on a high-fat diet. Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate, small molecules that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis..
Protein Sequence MPPAVGGPVGYTPPDGGWGWAVVIGAFISIGFSYAFPKSITVFFKEIEGIFHATTSEVSWISSIMLAVMYGGGPISSILVNKYGSRIVMIVGGCLSGCGLIAASFCNTVQQLYVCIGVIGGLGLAFNLNPALTMIGKYFYKRRPLANGLAMAGSPVFLCTLAPLNQVFFGIFGWRGSFLILGGLLLNCCVAGALMRPIGPKPTKAGKDKSKASLEKAGKSGVKKDLHDANTDLIGRHPKQEKRSVFQTINQFLDLTLFTHRGFLLYLSGNVIMFFGLFAPLVFLSSYGKSQHYSSEKSAFLLSILAFVDMVARPSMGLVANTKPIRPRIQYFFAASVVANGVCHMLAPLSTTYVGFCVYAGFFGFAFGWLSSVLFETLMDLVGPQRFSSAVGLVTIVECCPVLLGPPLLGRLNDMYGDYKYTYWACGVVLIISGIYLFIGMGINYRLLAKEQKANEQKKESKEEETSIDVAGKPNEVTKAAESPDQKDTDGGPKEEESPV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
11PhosphorylationAVGGPVGYTPPDGGW
CCCCCCCCCCCCCCC		19.1229438985
33PhosphorylationAFISIGFSYAFPKSI
EEEECCCHHCCCCEE		15.44-
34PhosphorylationFISIGFSYAFPKSIT
EEECCCHHCCCCEEE		15.25-
41PhosphorylationYAFPKSITVFFKEIE
HCCCCEEEEEEEEEC		20.5329438985
210PhosphorylationTKAGKDKSKASLEKA
CCCCCCHHHHHHHHH		43.5229396449
211UbiquitinationKAGKDKSKASLEKAG
CCCCCHHHHHHHHHH		47.97-
2112-HydroxyisobutyrylationKAGKDKSKASLEKAG
CCCCCHHHHHHHHHH		47.97-
213PhosphorylationGKDKSKASLEKAGKS
CCCHHHHHHHHHHHH		40.5726055452
216UbiquitinationKSKASLEKAGKSGVK
HHHHHHHHHHHHCCC		68.6721906983
220PhosphorylationSLEKAGKSGVKKDLH
HHHHHHHHCCCHHHH		48.1526074081
223UbiquitinationKAGKSGVKKDLHDAN
HHHHHCCCHHHHHCC		44.06-
224UbiquitinationAGKSGVKKDLHDANT
HHHHCCCHHHHHCCC		64.2221890473
224UbiquitinationAGKSGVKKDLHDANT
HHHHCCCHHHHHCCC		64.2221890473
224UbiquitinationAGKSGVKKDLHDANT
HHHHCCCHHHHHCCC		64.2221906983
231PhosphorylationKDLHDANTDLIGRHP
HHHHHCCCCCCCCCC		33.6228857561
239UbiquitinationDLIGRHPKQEKRSVF
CCCCCCCHHHHHHHH		66.03-
244PhosphorylationHPKQEKRSVFQTINQ
CCHHHHHHHHHHHHH		38.0521406692
248PhosphorylationEKRSVFQTINQFLDL
HHHHHHHHHHHHHHH		15.4921406692
256PhosphorylationINQFLDLTLFTHRGF
HHHHHHHHCCCCCCC		21.3521406692
259PhosphorylationFLDLTLFTHRGFLLY
HHHHHCCCCCCCHHH		17.4921406692
315PhosphorylationVDMVARPSMGLVANT
HHHHHCCCCCCCCCC		21.6720860994
450UbiquitinationINYRLLAKEQKANEQ
HHHHHHHHHHHHHHH		61.72-
4502-HydroxyisobutyrylationINYRLLAKEQKANEQ
HHHHHHHHHHHHHHH		61.72-
459UbiquitinationQKANEQKKESKEEET
HHHHHHHHHCHHHHH		67.9021906983
461PhosphorylationANEQKKESKEEETSI
HHHHHHHCHHHHHCC		55.0029255136
4622-HydroxyisobutyrylationNEQKKESKEEETSID
HHHHHHCHHHHHCCC		70.95-
462AcetylationNEQKKESKEEETSID
HHHHHHCHHHHHCCC		70.9523236377
462UbiquitinationNEQKKESKEEETSID
HHHHHHCHHHHHCCC		70.9521906983
466PhosphorylationKESKEEETSIDVAGK
HHCHHHHHCCCCCCC		33.9729255136
467PhosphorylationESKEEETSIDVAGKP
HCHHHHHCCCCCCCC		21.7729255136
473AcetylationTSIDVAGKPNEVTKA
HCCCCCCCCCHHCCH		34.6326051181
473UbiquitinationTSIDVAGKPNEVTKA
HCCCCCCCCCHHCCH		34.6321906983
478PhosphorylationAGKPNEVTKAAESPD
CCCCCHHCCHHCCCC		14.5923927012
479UbiquitinationGKPNEVTKAAESPDQ
CCCCHHCCHHCCCCC		51.2621890473
479UbiquitinationGKPNEVTKAAESPDQ
CCCCHHCCHHCCCCC		51.2621906983
483PhosphorylationEVTKAAESPDQKDTD
HHCCHHCCCCCCCCC		29.1123927012
487UbiquitinationAAESPDQKDTDGGPK
HHCCCCCCCCCCCCC		70.7221906983
489PhosphorylationESPDQKDTDGGPKEE
CCCCCCCCCCCCCCC		43.5123927012
494UbiquitinationKDTDGGPKEEESPV-
CCCCCCCCCCCCCC-		79.5821906983
494MethylationKDTDGGPKEEESPV-
CCCCCCCCCCCCCC-		79.5823644510
498PhosphorylationGGPKEEESPV-----
CCCCCCCCCC-----		33.9523927012
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of MOT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MOT1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MOT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CRBN_HUMANCRBNphysical
27294876
BASI_HUMANBSGphysical
27294876
Drug and Disease Associations
Kegg Disease
H01248 Erythrocyte lactate transporter defect
H01267 Familial hyperinsulinemic hypoglycemia (HHF)
OMIM Disease
245340Symptomatic deficiency in lactate transport (SDLT)
610021Familial hyperinsulinemic hypoglycemia 7 (HHF7)
616095Monocarboxylate transporter 1 deficiency (MCT1D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB03166Acetic acid
DB00345Aminohippurate
DB00415Ampicillin
DB00529Foscarnet
DB01440Gamma Hydroxybutyric Acid
DB00563Methotrexate
DB00731Nateglinide
DB00627Niacin
DB04552Niflumic Acid
DB00175Pravastatin
DB01032Probenecid
DB00119Pyruvic acid
DB00936Salicylic acid
DB00313Valproic Acid
Regulatory Network of MOT1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461; THR-466 ANDSER-498, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461; THR-466 ANDSER-467, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461; THR-466; SER-467;SER-483 AND SER-498, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461; SER-467; SER-483AND SER-498, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; THR-466; SER-467AND SER-498, AND MASS SPECTROMETRY.

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